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Serine/threonine-protein kinase akt-1 (EC 2.7.11.1) (Protein kinase B akt-1) (PKB akt-1)

 AKT1_CAEEL              Reviewed;         541 AA.
Q17941; Q17942; Q8MQE0;
24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
01-AUG-1998, sequence version 2.
22-NOV-2017, entry version 155.
RecName: Full=Serine/threonine-protein kinase akt-1;
EC=2.7.11.1;
AltName: Full=Protein kinase B akt-1;
Short=PKB akt-1;
Name=akt-1; ORFNames=C12D8.10;
Caenorhabditis elegans.
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
NCBI_TaxID=6239;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B), FUNCTION, MUTAGENESIS
OF ALA-183, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=9716402; DOI=10.1101/gad.12.16.2488;
Paradis S., Ruvkun G.;
"Caenorhabditis elegans Akt/PKB transduces insulin receptor-like
signals from AGE-1 PI3 kinase to the DAF-16 transcription factor.";
Genes Dev. 12:2488-2498(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE
SPLICING.
STRAIN=Bristol N2;
PubMed=9851916; DOI=10.1126/science.282.5396.2012;
The C. elegans sequencing consortium;
"Genome sequence of the nematode C. elegans: a platform for
investigating biology.";
Science 282:2012-2018(1998).
[3]
FUNCTION.
PubMed=10364160; DOI=10.1101/gad.13.11.1438;
Paradis S., Ailion M., Toker A., Thomas J.H., Ruvkun G.;
"A PDK1 homolog is necessary and sufficient to transduce AGE-1 PI3
kinase signals that regulate diapause in Caenorhabditis elegans.";
Genes Dev. 13:1438-1452(1999).
[4]
FUNCTION.
PubMed=11747825; DOI=10.1016/S0960-9822(01)00594-2;
Henderson S.T., Johnson T.E.;
"daf-16 integrates developmental and environmental inputs to mediate
aging in the nematode Caenorhabditis elegans.";
Curr. Biol. 11:1975-1980(2001).
[5]
FUNCTION.
PubMed=11381260; DOI=10.1038/88850;
Lin K., Hsin H., Libina N., Kenyon C.;
"Regulation of the Caenorhabditis elegans longevity protein DAF-16 by
insulin/IGF-1 and germline signaling.";
Nat. Genet. 28:139-145(2001).
[6]
FUNCTION, ENZYME REGULATION, INTERACTION WITH PDK-1; SGK-1; AKT-2 AND
DAF-16, AND DISRUPTION PHENOTYPE.
PubMed=15068796; DOI=10.1016/S1534-5807(04)00095-4;
Hertweck M., Goebel C., Baumeister R.;
"C. elegans SGK-1 is the critical component in the Akt/PKB kinase
complex to control stress response and life span.";
Dev. Cell 6:577-588(2004).
[7]
FUNCTION.
PubMed=16950159; DOI=10.1016/j.neuron.2006.07.024;
Tomioka M., Adachi T., Suzuki H., Kunitomo H., Schafer W.R., Iino Y.;
"The insulin/PI 3-kinase pathway regulates salt chemotaxis learning in
Caenorhabditis elegans.";
Neuron 51:613-625(2006).
[8]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=18782349; DOI=10.1111/j.1474-9726.2008.00435.x;
Evans E.A., Chen W.C., Tan M.-W.;
"The DAF-2 insulin-like signaling pathway independently regulates
aging and immunity in C. elegans.";
Aging Cell 7:879-893(2008).
[9]
FUNCTION.
PubMed=18358814; DOI=10.1016/j.cell.2008.01.030;
Tullet J.M., Hertweck M., An J.H., Baker J., Hwang J.Y., Liu S.,
Oliveira R.P., Baumeister R., Blackwell T.K.;
"Direct inhibition of the longevity-promoting factor SKN-1 by insulin-
like signaling in C. elegans.";
Cell 132:1025-1038(2008).
[10]
INTERACTION WITH CMD-1.
PubMed=17854888; DOI=10.1016/j.ceca.2007.07.008;
Shen X., Valencia C.A., Gao W., Cotten S.W., Dong B., Huang B.C.,
Liu R.;
"Ca(2+)/Calmodulin-binding proteins from the C. elegans proteome.";
Cell Calcium 43:444-456(2008).
[11]
INTERACTION WITH PPTR-1, TISSUE SPECIFICITY, AND PHOSPHORYLATION AT
THR-350 AND SER-517.
PubMed=19249087; DOI=10.1016/j.cell.2009.01.025;
Padmanabhan S., Mukhopadhyay A., Narasimhan S.D., Tesz G., Czech M.P.,
Tissenbaum H.A.;
"A PP2A regulatory subunit regulates C. elegans insulin/IGF-1
signaling by modulating AKT-1 phosphorylation.";
Cell 136:939-951(2009).
[12]
FUNCTION, DOMAIN, AND MUTAGENESIS OF ALA-183 AND LYS-222.
PubMed=25383666; DOI=10.1038/nsmb.2915;
Nakagawa A., Sullivan K.D., Xue D.;
"Caspase-activated phosphoinositide binding by CNT-1 promotes
apoptosis by inhibiting the AKT pathway.";
Nat. Struct. Mol. Biol. 21:1082-1090(2014).
-!- FUNCTION: Acts downstream of PI3 kinase age-1 and kinase pdk-1 in
the daf-2/insulin receptor-like transduction pathway.
Phosphorylates Forkhead-related daf-16 and the longevity-promoting
skn-1 transcription factors, which inhibits their entry into the
nucleus and antagonizes their functions (PubMed:9716402,
PubMed:11747825, PubMed:11381260, PubMed:15068796,
PubMed:18358814). Has an essential role in regulating
developmental arrest at the dauer stage (PubMed:10364160). Plays a
role in immune function and pathogen resistance (PubMed:18782349).
Regulates salt chemotaxis learning (PubMed:16950159). Downstream
of age-1 and together with akt-2 and sgk-1, promotes cell survival
during embryonic development (PubMed:25383666).
{ECO:0000269|PubMed:10364160, ECO:0000269|PubMed:11381260,
ECO:0000269|PubMed:11747825, ECO:0000269|PubMed:15068796,
ECO:0000269|PubMed:16950159, ECO:0000269|PubMed:18358814,
ECO:0000269|PubMed:18782349, ECO:0000269|PubMed:25383666,
ECO:0000269|PubMed:9716402}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
-!- ENZYME REGULATION: Phosphorylated and activated by pdk-1.
{ECO:0000269|PubMed:15068796}.
-!- SUBUNIT: Interacts with pdk-1, sgk-1, akt-2 and daf-16
(PubMed:15068796). Part of a complex containing sgk-1, akt-1 and
akt-2 (PubMed:15068796). Interacts with cmd-1 in the presence of
Ca(2+) (PubMed:17854888). Interacts with let-92 phosphatase
regulatory subunit pptr-1 (PubMed:19249087).
{ECO:0000269|PubMed:15068796, ECO:0000269|PubMed:17854888,
ECO:0000269|PubMed:19249087}.
-!- INTERACTION:
Q9XTG7:akt-2; NbExp=2; IntAct=EBI-1770718, EBI-320656;
O16850:daf-16; NbExp=3; IntAct=EBI-1770718, EBI-324028;
G5EFM0:mdf-1; NbExp=2; IntAct=EBI-1770718, EBI-316684;
O18178:pptr-1; NbExp=3; IntAct=EBI-1770718, EBI-2298122;
Q2PJ68:sgk-1; NbExp=3; IntAct=EBI-1770718, EBI-1770776;
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=a;
IsoId=Q17941-1; Sequence=Displayed;
Name=b;
IsoId=Q17941-2; Sequence=VSP_017044, VSP_017045, VSP_017046;
Name=c;
IsoId=Q17941-3; Sequence=VSP_038163;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in neurons, muscle cells of the
pharynx, rectal gland cells, vulva and spermatheca.
{ECO:0000269|PubMed:19249087, ECO:0000269|PubMed:9716402}.
-!- DEVELOPMENTAL STAGE: Expressed in late stage embryos and
throughout life. {ECO:0000269|PubMed:9716402}.
-!- DOMAIN: The PH domain binds to phosphatidylinositol 3,4,5-
trisphosphate (PtdIns(3,4,5)P3) resulting in its targeting to the
plasma membrane. {ECO:0000269|PubMed:25383666}.
-!- DISRUPTION PHENOTYPE: Increased resistance to pathogens.
Simultaneous knockdown of akt-1 and akt-2 result in dauer
formation and a weak extension to life span.
{ECO:0000269|PubMed:15068796, ECO:0000269|PubMed:18782349}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
protein kinase family. RAC subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF072379; AAC62466.1; -; mRNA.
EMBL; AF072380; AAC62467.1; -; mRNA.
EMBL; Z73969; CAA98238.1; -; Genomic_DNA.
EMBL; Z73969; CAA98240.1; -; Genomic_DNA.
EMBL; Z73969; CAD44085.1; -; Genomic_DNA.
PIR; T43232; T43232.
PIR; T43233; T43233.
RefSeq; NP_001023645.1; NM_001028474.4. [Q17941-1]
RefSeq; NP_001023646.1; NM_001028475.2.
RefSeq; NP_001023647.1; NM_001028476.3. [Q17941-3]
UniGene; Cel.5036; -.
ProteinModelPortal; Q17941; -.
SMR; Q17941; -.
BioGrid; 44454; 1.
IntAct; Q17941; 9.
STRING; 6239.C12D8.10b.1; -.
iPTMnet; Q17941; -.
EPD; Q17941; -.
PaxDb; Q17941; -.
PeptideAtlas; Q17941; -.
PRIDE; Q17941; -.
EnsemblMetazoa; C12D8.10a; C12D8.10a; WBGene00000102. [Q17941-1]
GeneID; 179424; -.
KEGG; cel:CELE_C12D8.10; -.
UCSC; C12D8.10b.1; c. elegans. [Q17941-1]
CTD; 179424; -.
WormBase; C12D8.10a; CE15612; WBGene00000102; akt-1. [Q17941-1]
WormBase; C12D8.10b; CE05274; WBGene00000102; akt-1. [Q17941-2]
WormBase; C12D8.10c; CE31304; WBGene00000102; akt-1. [Q17941-3]
eggNOG; KOG0598; Eukaryota.
eggNOG; ENOG410XNPH; LUCA.
GeneTree; ENSGT00890000139324; -.
HOGENOM; HOG000233033; -.
InParanoid; Q17941; -.
KO; K04456; -.
OMA; CQIMSVD; -.
OrthoDB; EOG091G06FF; -.
PhylomeDB; Q17941; -.
Reactome; R-CEL-114604; GPVI-mediated activation cascade.
Reactome; R-CEL-1257604; PIP3 activates AKT signaling.
Reactome; R-CEL-165158; Activation of AKT2.
Reactome; R-CEL-198323; AKT phosphorylates targets in the cytosol.
Reactome; R-CEL-198693; AKT phosphorylates targets in the nucleus.
Reactome; R-CEL-199418; Negative regulation of the PI3K/AKT network.
Reactome; R-CEL-211163; AKT-mediated inactivation of FOXO1A.
Reactome; R-CEL-389357; CD28 dependent PI3K/Akt signaling.
Reactome; R-CEL-392451; G beta:gamma signalling through PI3Kgamma.
Reactome; R-CEL-450385; Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA.
Reactome; R-CEL-450604; KSRP (KHSRP) binds and destabilizes mRNA.
Reactome; R-CEL-5218920; VEGFR2 mediated vascular permeability.
Reactome; R-CEL-6804758; Regulation of TP53 Activity through Acetylation.
Reactome; R-CEL-8876198; RAB GEFs exchange GTP for GDP on RABs.
Reactome; R-CEL-8948751; Regulation of PTEN stability and activity.
SignaLink; Q17941; -.
PRO; PR:Q17941; -.
Proteomes; UP000001940; Chromosome V.
Bgee; WBGene00000102; -.
GO; GO:0030424; C:axon; IDA:WormBase.
GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:WormBase.
GO; GO:0030425; C:dendrite; IDA:WormBase.
GO; GO:0005622; C:intracellular; IBA:GO_Central.
GO; GO:0043025; C:neuronal cell body; IDA:WormBase.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0005516; F:calmodulin binding; IDA:WormBase.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; IDA:WormBase.
GO; GO:0004672; F:protein kinase activity; IDA:WormBase.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:WormBase.
GO; GO:0007635; P:chemosensory behavior; IGI:UniProtKB.
GO; GO:0006935; P:chemotaxis; IGI:UniProtKB.
GO; GO:0008340; P:determination of adult lifespan; IMP:WormBase.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0008286; P:insulin receptor signaling pathway; IMP:WormBase.
GO; GO:0042771; P:intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IMP:CACAO.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:WormBase.
GO; GO:0018107; P:peptidyl-threonine phosphorylation; IDA:WormBase.
GO; GO:0006468; P:protein phosphorylation; IDA:WormBase.
GO; GO:0008582; P:regulation of synaptic growth at neuromuscular junction; IGI:UniProtKB.
GO; GO:1902074; P:response to salt; IGI:UniProtKB.
Gene3D; 2.30.29.30; -; 1.
InterPro; IPR000961; AGC-kinase_C.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR001849; PH_domain.
InterPro; IPR017892; Pkinase_C.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00169; PH; 1.
Pfam; PF00069; Pkinase; 1.
Pfam; PF00433; Pkinase_C; 1.
SMART; SM00233; PH; 1.
SMART; SM00133; S_TK_X; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF50729; SSF50729; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS51285; AGC_KINASE_CTER; 1.
PROSITE; PS50003; PH_DOMAIN; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Calmodulin-binding;
Complete proteome; Developmental protein; Immunity; Innate immunity;
Kinase; Lipid-binding; Magnesium; Metal-binding; Nucleotide-binding;
Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
Transferase.
CHAIN 1 541 Serine/threonine-protein kinase akt-1.
/FTId=PRO_0000085615.
DOMAIN 15 118 PH. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
DOMAIN 193 450 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 451 528 AGC-kinase C-terminal.
NP_BIND 199 207 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 316 316 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 222 222 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 350 350 Phosphothreonine.
{ECO:0000269|PubMed:19249087}.
MOD_RES 517 517 Phosphoserine.
{ECO:0000269|PubMed:19249087}.
VAR_SEQ 255 541 Missing (in isoform c). {ECO:0000305}.
/FTId=VSP_038163.
VAR_SEQ 262 287 EQHYLCFVMQFANGGELFTHVRKCGT -> TNDRLCFVMEF
AIGGDLYYHLNREVQMNKEG (in isoform b).
{ECO:0000303|PubMed:9716402}.
/FTId=VSP_017044.
VAR_SEQ 298 298 A -> S (in isoform b).
{ECO:0000303|PubMed:9716402}.
/FTId=VSP_017045.
VAR_SEQ 309 317 RCDIVYRDM -> ANSIVYRDL (in isoform b).
{ECO:0000303|PubMed:9716402}.
/FTId=VSP_017046.
MUTAGEN 183 183 A->T: In mg144; causes a delay in
apoptosis during embryonic development.
Suppresses the dauer arrest phenotype of
the age-1(mg44) null mutant.
{ECO:0000269|PubMed:25383666,
ECO:0000269|PubMed:9716402}.
MUTAGEN 222 222 K->M: Probable loss of kinase activity.
Increased apoptosis during embryonic
development in an akt-2 tm1075 mutant
background.
{ECO:0000269|PubMed:25383666}.
SEQUENCE 541 AA; 62200 MW; 17FEDD1109926950 CRC64;
MSMTSLSTKS RRQEDVVIEG WLHKKGEHIR NWRPRYFMIF NDGALLGFRA KPKEGQPFPE
PLNDFMIKDA ATMLFEKPRP NMFMVRCLQW TTVIERTFYA ESAEVRQRWI HAIESISKKY
KGTNANPQEE LMETNQQPKI DEDSEFAGAA HAIMGQPSSG HGDNCSIDFR ASMISIADTS
EAAKRDKITM EDFDFLKVLG KGTFGKVILC KEKRTQKLYA IKILKKDVII AREEVAHTLT
ENRVLQRCKH PFLTELKYSF QEQHYLCFVM QFANGGELFT HVRKCGTFSE PRARFYGAEI
VLALGYLHRC DIVYRDMKLE NLLLDKDGHI KIADFGLCKE EISFGDKTST FCGTPEYLAP
EVLDDHDYGR CVDWWGVGVV MYEMMCGRLP FYSKDHNKLF ELIMAGDLRF PSKLSQEART
LLTGLLVKDP TQRLGGGPED ALEICRADFF RTVDWEATYR KEIEPPYKPN VQSETDTSYF
DNEFTSQPVQ LTPPSRSGAL ATVDEQEEMQ SNFTQFSFHN VMGSINRIHE ASEDNEDYDM
G


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